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Database: UniProt
Entry: W9XHA3_9EURO
LinkDB: W9XHA3_9EURO
Original site: W9XHA3_9EURO 
ID   W9XHA3_9EURO            Unreviewed;       724 AA.
AC   W9XHA3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=E3 ubiquitin protein ligase {ECO:0000256|RuleBase:RU365038};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU365038};
GN   ORFNames=A1O3_07892 {ECO:0000313|EMBL:EXJ79613.1};
OS   Capronia epimyces CBS 606.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ79613.1, ECO:0000313|Proteomes:UP000019478};
RN   [1] {ECO:0000313|EMBL:EXJ79613.1, ECO:0000313|Proteomes:UP000019478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ79613.1,
RC   ECO:0000313|Proteomes:UP000019478};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU365038};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU365038}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365038}.
CC   -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000256|ARBA:ARBA00005555,
CC       ECO:0000256|RuleBase:RU365038}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ79613.1}.
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DR   EMBL; AMGY01000007; EXJ79613.1; -; Genomic_DNA.
DR   RefSeq; XP_007736187.1; XM_007737997.1.
DR   AlphaFoldDB; W9XHA3; -.
DR   STRING; 1182542.W9XHA3; -.
DR   GeneID; 19171987; -.
DR   eggNOG; KOG0978; Eukaryota.
DR   HOGENOM; CLU_019713_2_0_1; -.
DR   OrthoDB; 53681at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000019478; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16499; RING-HC_Bre1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR23163:SF0; E3 UBIQUITIN-PROTEIN LIGASE BRE1; 1.
DR   PANTHER; PTHR23163; RING FINGER PROTEIN-RELATED; 1.
DR   Pfam; PF08647; BRE1; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU365038};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU365038};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365038}; Nucleus {ECO:0000256|RuleBase:RU365038};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW   Transferase {ECO:0000256|RuleBase:RU365038};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU365038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365038};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          672..710
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          67..94
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          195..229
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          263..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          418..523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          629..656
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   724 AA;  82343 MW;  D7AA4C435780A7B4 CRC64;
     MTAVESLPPS LSHPSLVKME ERKRPSPYDQ VESAPPLKKQ ATSANGASKP HKDDDMPWKD
     DLERFQKDAI YRQMQEYRRE KNTLESQLKE MRKKARYHDD HLRIIDAWFQ QVIDEVKVMA
     KGDDDIDMDA SSLPSSLLFA DHDQFEEHLH NRSNEIKAVI STLFGPSKSL SADVTELQAR
     IARLLAAEKN HVVELSRLQA DKEDLEYRLE NASLRYMMAE KKIDRAKSVT VAKLEKQALL
     GATKPATEEG GPVKRDETAV NGATDHSEEL ADLEKELNKT VATAEKQKEQ LERLEEENAK
     LNEQLTELLT KSIILTDDDY AKTELFKQLK SQHEDVIKRI NNLEATNTEL REEAQKLRSE
     RTTFQLQLEN EARVAISERE SLLAASDANL ARIRHNRDEL LADQAVKKAT LEQDQEAVKK
     ITELASAQED RIKALESEKE RLSIQTSEMA VDNSELDAVS LEDLRTKYTE LEKKYNLLNG
     ELASMSTAYQ KTTRIAAQKV SEFAALEEKV MRLSAEKAKA DQKFFAAMKS KDTRDGEIRT
     LRLQNAKSAE AVSQLKEAEH ATRALLATME KQLSEMKDAL THKTNEHRTV QQQNVKQGLE
     VSRLNGQVTE LKNQLTAKDS KLATTSSLCR AAEVEVEELK SMLKDTRRSL ESWKSKSGQS
     EQYEMLRQFA YCNICKRALK NTVIKTCGHT FCNECVEERL TSRSRKCPNC GKSFGSNDHM
     RITL
//
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